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Journal Article

Cryogenic optical localization provides 3D protein structure data with Angstrom resolution.

MPS-Authors
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Schomburg,  B.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Giller,  K.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Supplementary Material (public)

2416986_Suppl_1.pdf
(Supplementary material), 3MB

2416986_Suppl_2.pdf
(Supplementary material), 73KB

Citation

Weisenburger, S., Boening, D., Schomburg, B., Giller, K., Becker, S., Griesinger, C., et al. (2017). Cryogenic optical localization provides 3D protein structure data with Angstrom resolution. Nature Methods, 14(2), 141-144. doi:10.1038/NMETH.4141.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002C-DE95-B
Abstract
We introduce Cryogenic Optical Localization in 3D (COLD), a method to localize multiple fluorescent sites within a single small protein with Angstrom resolution. We demonstrate COLD by determining the conformational state of the cytosolic Per-ARNT-Sim domain from the histidine kinase CitA of Geobacillus thermodenitnficans and resolving the four biotin sites of streptavidin. COLD provides quantitative 3D information about small- to medium-sized biomolecules on the Angstrom scale and complements other techniques in structural biology.